Weichbrodt, Conrad

[["dc.bibliographiccitation.firstpage","225"],["dc.bibliographiccitation.issue","S04"],["dc.bibliographiccitation.journal","Der Urologe"],["dc.bibliographiccitation.lastpage","228"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Ringert, R.-H."],["dc.contributor.author","Riedmiller, H."],["dc.contributor.author","Rübben, H."],["dc.contributor.author","Rose, A."],["dc.contributor.author","Hoyer, P. F."],["dc.contributor.author","Conrad, S."],["dc.contributor.author","Hoang-Böhm, J."],["dc.contributor.author","Müller-Wiefel, D. E."],["dc.date.accessioned","2021-06-01T10:49:05Z"],["dc.date.available","2021-06-01T10:49:05Z"],["dc.date.issued","2006"],["dc.identifier.doi","10.1007/s00120-006-1196-2"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86164"],["dc.language.iso","de"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1433-0563"],["dc.relation.issn","0340-2592"],["dc.title","Obstruktive Nephropathie"],["dc.title.translated","Obstructive nephropathy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9546"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Physical Chemistry Chemical Physics"],["dc.bibliographiccitation.lastpage","9555"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Kozuch, Jacek"],["dc.contributor.author","Weichbrodt, Conrad"],["dc.contributor.author","Millo, Diego"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Hildebrandt, Peter"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:46:55Z"],["dc.date.available","2017-09-07T11:46:55Z"],["dc.date.issued","2014"],["dc.description.abstract","The voltage-dependent anion channel (VDAC) is a transmembrane protein that regulates the transfer of metabolites between the cytosol and the mitochondrium. Opening and partial closing of the channel is known to be driven by the transmembrane potential via a mechanism that is not fully understood. In this work, we employed a spectroelectrochemical approach to probe the voltage-induced molecular structure changes of human VDAC1 (hVDAC1) embedded in a tethered bilayer lipid membrane on a nanostructured Au electrode. The model membrane consisted of a mixed self-assembled monolayer of 6-mercaptohexanol and (cholesterylpolyethylenoxy) thiol, followed by the deposition of 1-palmitoyl-2- oleoyl-sn-glycero-3-phosphocholine vesicles including hVDAC1. The stepwise assembly of the model membrane and the incorporation of hVDAC1 were monitored by surface enhanced infrared absorption and electrochemical impedance spectroscopy. Difference spectra allowed for identifying the spectral changes which may be associated with the transition from the open to the \"closed' states by shifting the potential above or below the transmembrane potential determined to be ca. 0.0 V vs. the open circuit potential. These spectral changes were interpreted on the basis of the orientation-and distancedependent IR enhancement and indicate alterations of the inclination angle of the beta-strands as crucial molecular events, reflecting an expansion or contraction of the beta-barrel pore. These protein structural changes that do not confirm nor exclude the reorientation of the alpha-helix are either directly induced by the electric field or a consequence of a potential-dependent repulsion or attraction of the bilayer."],["dc.identifier.doi","10.1039/c4cp00167b"],["dc.identifier.gro","3142210"],["dc.identifier.isi","000335818600039"],["dc.identifier.pmid","24728177"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5754"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1463-9084"],["dc.relation.issn","1463-9076"],["dc.title","Voltage-dependent structural changes of the membrane-bound anion channel hVDAC1 probed by SEIRA and electrochemical impedance spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4586"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","4591"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Song, Chen"],["dc.contributor.author","Weichbrodt, Conrad"],["dc.contributor.author","Salnikov, Evgeniy S."],["dc.contributor.author","Dynowski, Marek"],["dc.contributor.author","Forsberg, Björn O."],["dc.contributor.author","Bechinger, Burkhard"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Groot, Bert L. de"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Zeth, Kornelius"],["dc.date.accessioned","2017-09-07T11:47:46Z"],["dc.date.available","2017-09-07T11:47:46Z"],["dc.date.issued","2013"],["dc.description.abstract","Multicellular organisms fight bacterial and fungal infections by producing peptide-derived broad-spectrum antibiotics. These host-defense peptides compromise the integrity of microbial cell membranes and thus evade pathways by which bacteria develop rapid antibiotic resistance. Although more than 1,700 host-defense peptides have been identified, the structural and mechanistic basis of their action remains speculative. This impedes the desired rational development of these agents into next-generation antibiotics. We present the X-ray crystal structure as well as solid-state NMR spectroscopy, electrophysiology, and MD simulations of human dermcidin in membranes that reveal the antibiotic mechanism of this major human antimicrobial, found to suppress Staphylococcus aureus growth on the epidermal surface. Dermcidin forms an architecture of high-conductance transmembrane channels, composed of zinc-connected trimers of antiparallel helix pairs. Molecular dynamics simulations elucidate the unusual membrane permeation pathway for ions and show adjustment of the pore to various membranes. Our study unravels the comprehensive mechanism for the membrane-disruptive action of this mammalian host-defense peptide at atomistic level. The results may form a foundation for the structure-based design of peptide antibiotics."],["dc.identifier.doi","10.1073/pnas.1214739110"],["dc.identifier.gro","3142374"],["dc.identifier.isi","000317521600044"],["dc.identifier.pmid","23426625"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7575"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Crystal structure and functional mechanism of a human antimicrobial membrane channel"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1223"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","1234"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Briones, Rodolfo"],["dc.contributor.author","Weichbrodt, Conrad"],["dc.contributor.author","Paltrinieri, Licia"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Villinger, Saskia"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Lange, Adam"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","De Groot, Bert L."],["dc.date.accessioned","2017-09-07T11:44:37Z"],["dc.date.available","2017-09-07T11:44:37Z"],["dc.date.issued","2016"],["dc.description.abstract","The voltage-dependent anion channel 1 (VDAC-1) is an important protein of the outer mitochondria! membrane that transports energy metabolites and is involved in apoptosis. The available structures of VDAC proteins show a wide beta-stranded barrel pore, with its N-terminal alpha-helix (N-alpha) bound to its interior. Electrophysiology experiments revealed that voltage, its polarity, and membrane composition modulate VDAC currents. Experiments with VDAC-1 mutants identified amino acids that regulate the gating process. However, the mechanisms for how these factors regulate VDAC-1, and which changes they trigger in the channel, are still unknown. In this study, molecular dynamics simulations and single-channel experiments of VDAC-1 show agreement for the current-voltage relationships of an \"open\" channel and they also show several subconducting transient states that are more cation selective in the simulations. We observed voltage-dependent asymmetric distortions of the VDAC-1 barrel and the displacement of particular charged amino acids. We constructed conformational models of the protein voltage response and the pore changes that consistently explain the protein conformations observed at opposite voltage polarities, either in phosphatidylethanolamine or phosphatidylcholine membranes. The submicrosecond VDAC-1 voltage response shows intrinsic structural changes that explain the role of key gating amino acids and support some of the current gating hypotheses. These voltage-dependent protein changes include asymmetric barrel distortion, its interaction with the membrane, and significant displacement of N-alpha amino acids."],["dc.identifier.doi","10.1016/j.bpj.2016.08.007"],["dc.identifier.gro","3141619"],["dc.identifier.isi","000383925700015"],["dc.identifier.pmid","27653481"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13769"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1900"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Voltage Dependence of Conformational Dynamics and Subconducting States of VDAC-1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Weichbrodt, Conrad"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2018-11-07T08:53:37Z"],["dc.date.available","2018-11-07T08:53:37Z"],["dc.date.issued","2011"],["dc.format.extent","173"],["dc.identifier.isi","000293637300461"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22459"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New York"],["dc.relation.eventlocation","Budapest, Hungary"],["dc.relation.issn","0175-7571"],["dc.title","Electrophysiological investigation of the hVDAC1 ion channel in pore-spanning membranes"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3347"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","Soft Matter"],["dc.bibliographiccitation.lastpage","3353"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Schmitt, Eva K."],["dc.contributor.author","Weichbrodt, Conrad"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:47:36Z"],["dc.date.available","2017-09-07T11:47:36Z"],["dc.date.issued","2009"],["dc.description.abstract","Porous alumina substrates with a pore diameter of 60 nm were functionalized with cholesterylpolyethylenoxy thiol (CPEO3) chemisorbed on gold, which is a prerequisite for the formation of pore-suspending membranes obtained from spreading of large unilamellar vesicles with a mean diameter of 730 nm. By means of vesicle fusion, a large number of gramicidin D ion channels, selective for monovalent cations, was successfully reconstituted into these pore-suspending membranes as probed by impedance spectroscopy. An electrical equivalent circuit was developed to fully describe the electrical properties of the gramicidin D-doped membrane system, which allowed us not only to extract the membrane resistance but also the mass transport in bulk solution as a function of the monovalent cation concentration in solution. Blocking of channel activity was demonstrated by the addition of Ca(2+) ions verifying the reconstitution of fully functional peptides."],["dc.identifier.doi","10.1039/b901683j"],["dc.identifier.gro","3143185"],["dc.identifier.isi","000269062900022"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/671"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: DFG [STE 552/8]; Fonds der Chemischen Industrie for a PhD fellowship"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1744-683X"],["dc.title","Impedance analysis of gramicidin D in pore-suspending membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","241a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Song, Chen"],["dc.contributor.author","Weichbrodt, Conrad"],["dc.contributor.author","Dynowski, Marek"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Zeth, Kornelius"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Forsberg, Björn O."],["dc.date.accessioned","2018-11-07T09:28:59Z"],["dc.date.available","2018-11-07T09:28:59Z"],["dc.date.issued","2013"],["dc.format.extent","241A"],["dc.identifier.doi","10.1016/j.bpj.2012.11.1359"],["dc.identifier.isi","000316074302239"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30915"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.eventlocation","Philadelphia, PA"],["dc.relation.issn","0006-3495"],["dc.title","Channel Crystal Structure and Antimicrobial Mechanism of Dermcidin from Human Skin"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]